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HPRT_BUCAI
ID   HPRT_BUCAI              Reviewed;         178 AA.
AC   P57291;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Hypoxanthine phosphoribosyltransferase;
DE            Short=HPRT;
DE            EC=2.4.2.8 {ECO:0000250|UniProtKB:P0A9M2};
GN   Name=hpt; OrderedLocusNames=BU195;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
CC   -!- FUNCTION: Purine salvage pathway enzyme which catalyzes the transfer of
CC       the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-
CC       diphosphate (PRPP) to the N9 position of hypoxanthine to yield IMP
CC       (inosine 5'-monophosphate). To a lesser extent, can also act on guanine
CC       leading to GMP, but shows a highly less efficient activity with
CC       xanthine. {ECO:0000250|UniProtKB:P0A9M2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC         hypoxanthine; Xref=Rhea:RHEA:17973, ChEBI:CHEBI:17368,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58053; EC=2.4.2.8;
CC         Evidence={ECO:0000250|UniProtKB:P0A9M2};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975;
CC         Evidence={ECO:0000250|UniProtKB:P0A9M2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + GMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC         guanine; Xref=Rhea:RHEA:25424, ChEBI:CHEBI:16235, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58017, ChEBI:CHEBI:58115; EC=2.4.2.8;
CC         Evidence={ECO:0000250|UniProtKB:P0A9M2};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426;
CC         Evidence={ECO:0000250|UniProtKB:P0A9M2};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P0A9M2};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC       from hypoxanthine: step 1/1. {ECO:0000250|UniProtKB:P0A9M2}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0A9M2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB12912.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BA000003; BAB12912.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; NP_240026.1; NC_002528.1.
DR   AlphaFoldDB; P57291; -.
DR   SMR; P57291; -.
DR   STRING; 107806.10038877; -.
DR   EnsemblBacteria; BAB12912; BAB12912; BAB12912.
DR   KEGG; buc:BU195; -.
DR   PATRIC; fig|107806.10.peg.206; -.
DR   eggNOG; COG0634; Bacteria.
DR   HOGENOM; CLU_073615_0_0_6; -.
DR   OMA; IEFMAVS; -.
DR   UniPathway; UPA00591; UER00648.
DR   Proteomes; UP000001806; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   InterPro; IPR005904; Hxn_phspho_trans.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR01203; HGPRTase; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycosyltransferase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Purine salvage; Reference proteome; Transferase.
FT   CHAIN           1..178
FT                   /note="Hypoxanthine phosphoribosyltransferase"
FT                   /id="PRO_0000139630"
FT   REGION          43..44
FT                   /note="Diphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT   ACT_SITE        103
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT   BINDING         99
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT   BINDING         99
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT   BINDING         99
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT   BINDING         100
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT   BINDING         103..108
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT   BINDING         103..108
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT   BINDING         131
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT   BINDING         131
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT   BINDING         160
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT   BINDING         166
FT                   /ligand="diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:33019"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHQ9"
SQ   SEQUENCE   178 AA;  20593 MW;  D79B7A06E5E2C350 CRC64;
     MKHTLQVIIT EKELDIRVRE LGQEITKKYR NSRNKMILIA LLRGSFIFIS DLCRRIHIEH
     EIDFMTTSSY GRGMLSSGDV KIIKDLDEDI YNKNVLIVED IIDSGKTLSK VLDILKLRNP
     KSLSICTLLD KPECREVNIN VDFIGFSILE NFFIVGYGID YAQSYRYLPN IGKVVFKK
 
 
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